Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Calcein leakage after 5 minutes from ( A ) anionic, bacteria-mimetic POPE/POPG (7:3) LUVs and ( B ) zwitterionic, erythrocyte-mimetic POPC/cholesterol (2:1) LUVs. ( C ) Depolarization of E. coli ATCC 35218 after 5-min. treatment, as monitored by diSC3-5 fluorescence. The data are representative of 3 independent experiments.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Bacteria, Fluorescence

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: In vitro activities of peptoids and peptides.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: In Vitro, Sequencing

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Scanning electron micrographs of E. coli either ( A ) without treatment, or treated for one hour with 10 μM ( B ) peptoid 1 ( C ) 1-Pro 6 , ( D ) 1 17mer , ( E ) peptoid 2, ( F ) 1 17mer alone (no bacteria), ( G ) pexiganan, or ( H ) melittin. Magnification = 50,000X.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Bacteria

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Comparison of transmission electron micrographs of transverse thin sections of representative E. coli treated for 1 hour with enough peptide or peptoid to kill some, but not all of the bacteria in the sample. ( A ) No treatment, ( B ) 10 µM pexiganan, ( C ) 100 µM melittin, ( D ) 10 µM fowlicidin-1, ( E ) 10 µM LL-37, ( F ) 10 µM peptoid 1, ( G ) 100 µM 1- N Lys 5,11 , ( H ) 100 µM 1-Pro 6 , ( I ) 10 µM 1 17mer . Images of bacteria treated with 2, 1 achiral , and 1- N sna 6,12 , are shown in Supp. Fig. . Scale bar represents 100 nm.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Comparison, Transmission Assay, Bacteria

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Transmission electron micrographs demonstrating the co-incidence of altered and control-like morphologies in partially killed samples treated with ( A ) 10 µM LL-37 and ( B ) 10 µM peptoid 1. Soft x-ray tomography of E. coli . ( C ) Control (untreated) and ( D ) treated with 10 µM peptoid 1. Scale bar (TEM) represents 100 nm.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Transmission Assay, Control, Tomography

Journal: Scientific Reports

Article Title: Intracellular biomass flocculation as a key mechanism of rapid bacterial killing by cationic, amphipathic antimicrobial peptides and peptoids

doi: 10.1038/s41598-017-16180-0

Figure Lengend Snippet: Transmission electron micrographs of E. coli treated with 100 µM peptoid 1 for ( A ) 5 minutes, ( B ) 15 minutes, ( C ) 30 minutes, and ( D ) 1 hour. 1 × 10 4 CFU/mL bacteria remained (0.01% of bacteria in the control) after 5-min treatment; all bacteria were killed after 15-min, 30-min, and 60-min treatments. Scale bar represents 100 nm.

Article Snippet: The top portion of Table lists the two peptides (pexiganan, an analog of magainin, and bee venom-derived melittin, whose membrane-disruptive activities are well-documented , ) and the peptoids used for these studies, along with their sequences (see Fig. for a guide to peptoid monomers), antibacterial activities against E. coli ATCC 35218, and hemolytic activities.

Techniques: Transmission Assay, Bacteria, Control